TDIF2_HUMAN
ID TDIF2_HUMAN Reviewed; 756 AA.
AC Q5QJE6; Q12987; Q53H59; Q5TFJ4; Q6TLI0; Q76MJ8; Q86WX9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Deoxynucleotidyltransferase terminal-interacting protein 2;
DE AltName: Full=Estrogen receptor-binding protein;
DE AltName: Full=LPTS-interacting protein 2;
DE Short=LPTS-RP2;
DE AltName: Full=Terminal deoxynucleotidyltransferase-interacting factor 2;
DE Short=TdIF2;
DE Short=TdT-interacting factor 2;
GN Name=DNTTIP2; Synonyms=ERBP, TDIF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309, FUNCTION, IDENTIFICATION IN A
RP COMPLEX WITH DNTT; PCNA AND CORE HISTONE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=12786946; DOI=10.1046/j.1365-2443.2003.00656.x;
RA Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K.,
RA Fujisaki S., Hayano T., Koiwai O.;
RT "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel
RT chromatin remodeling protein with 82 kDa and core histone.";
RL Genes Cells 8:559-571(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; ESR2; PPARG
RP AND RXRA, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
RA Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
RA Zhu Y.-J.;
RT "ERBP, a novel estrogen receptor binding protein enhancing the activity of
RT estrogen receptor.";
RL Biochem. Biophys. Res. Commun. 317:54-59(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Carlsson P.;
RT "cDNA encoding an acidic 82 kDa protein.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-309.
RC TISSUE=Liver;
RA Song H., Zhao M., Li T.;
RT "LPTS-RP2, one LPTS-interacting protein.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-309.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-309.
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; THR-129;
RP SER-141; SER-145; SER-148; SER-184; SER-194; THR-232; SER-324 AND SER-381,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; SER-141;
RP THR-232; SER-251; SER-330; SER-434; SER-512 AND THR-610, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-434 AND SER-512, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-141; THR-232;
RP SER-239; SER-251; SER-253; SER-330 AND SER-569, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-558; LYS-626; LYS-649; LYS-658
RP AND LYS-686, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-558; LYS-626 AND LYS-658, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217; LYS-220; LYS-257; LYS-316;
RP LYS-321; LYS-345; LYS-384; LYS-558; LYS-584; LYS-606; LYS-626; LYS-649;
RP LYS-658; LYS-686 AND LYS-731, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May
CC function as a chromatin remodeling protein.
CC {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.
CC -!- SUBUNIT: Forms a ternary complex with DNTT and core histone;
CC interaction with PCNA releases DNTT and H2A/H2B histones from this
CC ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA.
CC {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.
CC -!- INTERACTION:
CC Q5QJE6; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-5666736, EBI-2559016;
CC Q5QJE6; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-5666736, EBI-739624;
CC Q5QJE6; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5666736, EBI-79165;
CC Q5QJE6; O76064: RNF8; NbExp=3; IntAct=EBI-5666736, EBI-373337;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12786946,
CC ECO:0000269|PubMed:15047147}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher levels in testis.
CC {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50601.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH47688.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB046574; BAD08331.1; -; mRNA.
DR EMBL; AY394925; AAQ95169.1; -; mRNA.
DR EMBL; U15552; AAA50601.1; ALT_FRAME; mRNA.
DR EMBL; AY336729; AAR02407.1; -; mRNA.
DR EMBL; AK292379; BAF85068.1; -; mRNA.
DR EMBL; AK222722; BAD96442.1; -; mRNA.
DR EMBL; AL049796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73064.1; -; Genomic_DNA.
DR EMBL; BC047688; AAH47688.1; ALT_SEQ; mRNA.
DR EMBL; BC130622; AAI30623.1; -; mRNA.
DR CCDS; CCDS44174.1; -.
DR PIR; G01522; G01522.
DR RefSeq; NP_055412.2; NM_014597.4.
DR PDB; 7MQ8; EM; 3.60 A; SQ=1-756.
DR PDB; 7MQ9; EM; 3.87 A; SQ=1-756.
DR PDB; 7MQA; EM; 2.70 A; SQ=1-756.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q5QJE6; -.
DR SMR; Q5QJE6; -.
DR BioGRID; 119052; 118.
DR CORUM; Q5QJE6; -.
DR IntAct; Q5QJE6; 26.
DR MINT; Q5QJE6; -.
DR STRING; 9606.ENSP00000411010; -.
DR GlyGen; Q5QJE6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5QJE6; -.
DR PhosphoSitePlus; Q5QJE6; -.
DR BioMuta; DNTTIP2; -.
DR DMDM; 166987398; -.
DR EPD; Q5QJE6; -.
DR jPOST; Q5QJE6; -.
DR MassIVE; Q5QJE6; -.
DR MaxQB; Q5QJE6; -.
DR PaxDb; Q5QJE6; -.
DR PeptideAtlas; Q5QJE6; -.
DR PRIDE; Q5QJE6; -.
DR ProteomicsDB; 63620; -.
DR Antibodypedia; 48013; 21 antibodies from 8 providers.
DR DNASU; 30836; -.
DR Ensembl; ENST00000436063.7; ENSP00000411010.2; ENSG00000067334.14.
DR GeneID; 30836; -.
DR KEGG; hsa:30836; -.
DR MANE-Select; ENST00000436063.7; ENSP00000411010.2; NM_014597.5; NP_055412.2.
DR UCSC; uc001dqf.4; human.
DR CTD; 30836; -.
DR DisGeNET; 30836; -.
DR GeneCards; DNTTIP2; -.
DR HGNC; HGNC:24013; DNTTIP2.
DR HPA; ENSG00000067334; Low tissue specificity.
DR MIM; 611199; gene.
DR neXtProt; NX_Q5QJE6; -.
DR OpenTargets; ENSG00000067334; -.
DR PharmGKB; PA142671963; -.
DR VEuPathDB; HostDB:ENSG00000067334; -.
DR eggNOG; KOG3100; Eukaryota.
DR GeneTree; ENSGT00510000048142; -.
DR HOGENOM; CLU_018725_0_0_1; -.
DR InParanoid; Q5QJE6; -.
DR OMA; SENMSCD; -.
DR OrthoDB; 887634at2759; -.
DR PhylomeDB; Q5QJE6; -.
DR TreeFam; TF105964; -.
DR PathwayCommons; Q5QJE6; -.
DR SignaLink; Q5QJE6; -.
DR BioGRID-ORCS; 30836; 482 hits in 1102 CRISPR screens.
DR ChiTaRS; DNTTIP2; human.
DR GeneWiki; DNTTIP2; -.
DR GenomeRNAi; 30836; -.
DR Pharos; Q5QJE6; Tdark.
DR PRO; PR:Q5QJE6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5QJE6; protein.
DR Bgee; ENSG00000067334; Expressed in calcaneal tendon and 201 other tissues.
DR ExpressionAtlas; Q5QJE6; baseline and differential.
DR Genevisible; Q5QJE6; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR InterPro; IPR039883; Fcf2/DNTTIP2.
DR InterPro; IPR014810; Fcf2_C.
DR PANTHER; PTHR21686; PTHR21686; 2.
DR Pfam; PF08698; Fcf2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..756
FT /note="Deoxynucleotidyltransferase terminal-interacting
FT protein 2"
FT /id="PRO_0000318505"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..605
FT /note="TdBR region; mediates interaction with DNTT"
FT COILED 505..542
FT /evidence="ECO:0000255"
FT COMPBIAS 10..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 606
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 626
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 309
FT /note="E -> D (in dbSNP:rs3747965)"
FT /evidence="ECO:0000269|PubMed:12786946,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.8"
FT /id="VAR_038748"
FT VARIANT 341
FT /note="T -> A (in dbSNP:rs3179879)"
FT /id="VAR_038749"
FT VARIANT 430
FT /note="A -> V (in dbSNP:rs35650636)"
FT /id="VAR_038750"
FT VARIANT 477
FT /note="G -> E (in dbSNP:rs41292661)"
FT /id="VAR_061710"
FT VARIANT 676
FT /note="Y -> F (in dbSNP:rs12748154)"
FT /id="VAR_038751"
FT CONFLICT 47
FT /note="A -> D (in Ref. 2; AAQ95169 and 3; AAA50601)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="R -> S (in Ref. 2; AAQ95169 and 3; AAA50601)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="M -> I (in Ref. 6; BAD96442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 84469 MW; 5C58EFABA2B42E4B CRC64;
MVVTRSARAK ASIQAASAES SGQKSFAANG IQAHPESSTG SDARTTAESQ TTGKQSLIPR
TPKARKRKSR TTGSLPKGTE PSTDGETSEA ESNYSVSEHH DTILRVTRRR QILIACSPVS
SVRKKPKVTP TKESYTEEIV SEAESHVSGI SRIVLPTEKT TGARRSKAKS LTDPSQESHT
EAISDAETSS SDISFSGIAT RRTRSMQRKL KAQTEKKDSK IVPGNEKQIV GTPVNSEDSD
TRQTSHLQAR SLSEINKPNF YNNDFDDDFS HRSSENILTV HEQANVESLK ETKQNCKDLD
EDANGITDEG KEINEKSSQL KNLSELQDTS LQQLVSQRHS TPQNKNAVSV HSNLNSEAVM
KSLTQTFATV EVGRWNNNKK SPIKASDLTK FGDCGGSDDE EESTVISVSE DMNSEGNVDF
ECDTKLYTSA PNTSQGKDNS VLLVLSSDES QQSENSENEE DTLCFVENSG QRESLSGDTG
SLSCDNALFV IDTTPGMSAD KNFYLEEEDK ASEVAIEEEK EEEEDEKSEE DSSDHDENED
EFSDEEDFLN STKAKLLKLT SSSIDPGLSI KQLGGLYINF NADKLQSNKR TLTQIKEKKK
NELLQKAVIT PDFEKNHCVP PYSESKYQLQ KKRRKERQKT AGDGWFGMKA PEMTNELKND
LKALKMRASM DPKRFYKKND RDGFPKYFQI GTIVDNPADF YHSRIPKKQR KRTIVEELLA
DSEFRRYNRR KYSEIMAEKA ANAAGKKFRK KKKFRN
